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Q15149

- PLEC_HUMAN

UniProt

Q15149 - PLEC_HUMAN

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Protein

Plectin

Gene

PLEC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofibers integrity.2 Publications

GO - Molecular functioni

  1. ankyrin binding Source: BHF-UCL
  2. poly(A) RNA binding Source: UniProtKB
  3. structural constituent of muscle Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cell junction assembly Source: Reactome
  3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  4. extracellular matrix organization Source: Reactome
  5. hemidesmosome assembly Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_20537. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Plectin
Short name:
PCN
Short name:
PLTN
Alternative name(s):
Hemidesmosomal protein 1
Short name:
HD1
Plectin-1
Gene namesi
Name:PLEC
Synonyms:PLEC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:9069. PLEC.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cell junctionhemidesmosome 1 Publication

GO - Cellular componenti

  1. costamere Source: BHF-UCL
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. focal adhesion Source: UniProtKB
  6. hemidesmosome Source: UniProtKB
  7. intermediate filament cytoskeleton Source: HPA
  8. plasma membrane Source: ProtInc
  9. sarcolemma Source: UniProtKB
  10. sarcoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Epidermolysis bullosa simplex with pyloric atresia (EBS-PA) [MIM:612138]: Autosomal recessive genodermatosis characterized by severe skin blistering at birth and congenital pyloric atresia. Death usually occurs in infancy. This disorder is allelic to MD-EBS.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Epidermolysis bullosa simplex, with muscular dystrophy (MD-EBS) [MIM:226670]: A form of epidermolysis bullosa characterized by the association of blister formation at the level of the hemidesmosome with late-onset muscular dystrophy.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti429 – 4291L → LL in MD-EBS. 1 Publication
VAR_011336
Natural varianti1003 – 10053Missing in MD-EBS. 1 Publication
VAR_011337
Epidermolysis bullosa simplex, Ogna type (O-EBS) [MIM:131950]: A form of intraepidermal epidermolysis bullosa characterized by generalized skin bruising, skin fragility with non-scarring blistering and small hemorrhagic blisters on hands. At the ultrastructural level, it is differentiated from classical cases of K-EBS, WC-EBS and DM-EBS, by the occurrence of blisters originating in basal cells above hemidesmosomes, and abnormal hemidesmosome intracellular attachment plates.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2110 – 21101R → W in O-EBS. 1 Publication
VAR_015817
Limb-girdle muscular dystrophy 2Q (LGMD2Q) [MIM:613723]: A form of limb-girdle muscular dystrophy characterized by early childhood onset of proximal muscle weakness. Limb-girdle muscular dystrophies are characterized by proximal weakness, weakness of the hip and shoulder girdles and prominent asymmetrical quadriceps femoris and biceps brachii atrophy.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry. A 9 bp deletion containing the initiation codon in exon 1f of PLEC have been found in limb-girdle muscular dystrophy patients. The mutation results in deficient expression of isoform 9 and disorganization of the myofibers, without any effect on the skin.

Keywords - Diseasei

Disease mutation, Epidermolysis bullosa, Limb-girdle muscular dystrophy

Organism-specific databases

MIMi131950. phenotype.
226670. phenotype.
612138. phenotype.
613723. phenotype.
Orphaneti254361. Autosomal recessive limb-girdle muscular dystrophy type 2Q.
257. Epidermolysis bullosa simplex with muscular dystrophy.
158684. Epidermolysis bullosa simplex with pyloric atresia.
79401. Epidermolysis bullosa simplex, Ogna type.
PharmGKBiPA33399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 46844684PlectinPRO_0000078135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131Phosphothreonine1 Publication
Modified residuei125 – 1251Phosphoserine3 Publications
Modified residuei149 – 1491Phosphoserine3 Publications
Modified residuei720 – 7201Phosphoserine4 Publications
Modified residuei1435 – 14351Phosphoserine4 Publications
Modified residuei1721 – 17211Phosphoserine1 Publication
Modified residuei1725 – 17251N6-acetyllysineBy similarity
Modified residuei1732 – 17321Phosphoserine1 Publication
Modified residuei2636 – 26361N6-acetyllysineBy similarity
Modified residuei3033 – 30331PhosphotyrosineBy similarity
Modified residuei3053 – 30531N6-acetyllysineBy similarity
Modified residuei3091 – 30911N6-acetyllysine1 Publication
Modified residuei3362 – 33621PhosphotyrosineBy similarity
Modified residuei3420 – 34201N6-acetyllysine1 Publication
Modified residuei4030 – 40301Phosphothreonine4 Publications
Modified residuei4382 – 43821Phosphoserine2 Publications
Modified residuei4384 – 43841PhosphoserineBy similarity
Modified residuei4385 – 43851Phosphoserine2 Publications
Modified residuei4386 – 43861Phosphoserine2 Publications
Modified residuei4389 – 43891Phosphoserine2 Publications
Modified residuei4390 – 43901Phosphoserine1 Publication
Modified residuei4391 – 43911Phosphoserine1 Publication
Modified residuei4392 – 43921Phosphoserine1 Publication
Modified residuei4396 – 43961Phosphoserine3 Publications
Modified residuei4400 – 44001Phosphoserine1 Publication
Modified residuei4411 – 44111Phosphothreonine1 Publication
Modified residuei4539 – 45391Phosphothreonine; by CDK1By similarity
Modified residuei4613 – 46131Phosphoserine3 Publications
Modified residuei4615 – 46151PhosphotyrosineBy similarity
Modified residuei4618 – 46181Phosphoserine1 Publication
Modified residuei4622 – 46221Phosphoserine2 Publications
Modified residuei4626 – 46261Phosphoserine3 Publications
Modified residuei4642 – 46421Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated by CDK1; regulates dissociation from intermediate filaments during mitosis.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15149.
PaxDbiQ15149.
PRIDEiQ15149.

PTM databases

PhosphoSiteiQ15149.

Expressioni

Tissue specificityi

Widely expressed with highest levels in muscle, heart, placenta and spinal cord.

Gene expression databases

BgeeiQ15149.
CleanExiHS_PLEC1.
ExpressionAtlasiQ15149. baseline and differential.
GenevestigatoriQ15149.

Organism-specific databases

HPAiCAB003847.
HPA025967.
HPA029906.

Interactioni

Subunit structurei

Homodimer or homotetramer. Interacts (via actin-binding domain) with SYNE3. Interacts (via CH 1 domain) with VIM (via rod region). Interacts (via N-terminus) with DST isoform 2 (via N-terminus). Interacts with FER. Interacts with TOR1A. Interacts with ANK3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FUSP356374EBI-297903,EBI-400434
ITGB4P161447EBI-297903,EBI-948678

Protein-protein interaction databases

BioGridi111355. 62 interactions.
IntActiQ15149. 25 interactions.
MINTiMINT-257064.

Structurei

Secondary structure

1
4684
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi175 – 19319
Helixi194 – 1963
Turni203 – 2097
Helixi211 – 22111
Helixi233 – 24917
Helixi260 – 2634
Helixi267 – 28216
Helixi297 – 30812
Turni309 – 3113
Helixi322 – 3243
Helixi328 – 33710
Helixi339 – 3413
Helixi344 – 3474
Helixi352 – 36716
Helixi375 – 3784
Beta strandi380 – 3823
Helixi385 – 39814
Helixi414 – 44027
Helixi448 – 46417
Helixi466 – 48823
Beta strandi490 – 4923
Helixi500 – 56263
Turni563 – 5664
Helixi572 – 59827
Helixi604 – 62825
Helixi656 – 67823
Helixi685 – 71430
Helixi715 – 7184
Helixi721 – 77858
Helixi788 – 82134
Helixi827 – 85428
Helixi893 – 9008
Helixi904 – 92522
Helixi932 – 9343
Beta strandi944 – 9485
Beta strandi964 – 9707
Beta strandi975 – 9795
Beta strandi985 – 9895
Helixi990 – 9923
Helixi1000 – 102425
Helixi1493 – 152735

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MB8X-ray2.15A175-403[»]
2ODUX-ray2.30A410-640[»]
2ODVX-ray2.05A410-640[»]
3F7PX-ray2.75A/B175-403[»]
3PDYX-ray2.22A/B653-858[»]
3PE0X-ray2.95A/B750-1028[»]
4GDOX-ray1.70A/B/C/D/E/F1492-1530[»]
4Q58X-ray4.00A/B175-400[»]
4Q59X-ray2.30A/B175-400[»]
ProteinModelPortaliQ15149.
SMRiQ15149. Positions 5-101, 175-400, 413-630, 653-1025, 2782-3023, 3441-3681, 4021-4260, 4412-4605.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15149.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini175 – 400226Actin-bindingAdd
BLAST
Domaini179 – 282104CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini295 – 397103CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati645 – 71066Spectrin 1Add
BLAST
Repeati740 – 82485Spectrin 2Add
BLAST
Repeati837 – 93094Spectrin 3Add
BLAST
Repeati1315 – 1415101Spectrin 4Add
BLAST
Repeati2826 – 286338Plectin 1Add
BLAST
Repeati2864 – 290138Plectin 2Add
BLAST
Repeati2902 – 293938Plectin 3Add
BLAST
Repeati2940 – 297738Plectin 4Add
BLAST
Repeati2981 – 301535Plectin 5Add
BLAST
Repeati3116 – 315338Plectin 6Add
BLAST
Repeati3154 – 319138Plectin 7Add
BLAST
Repeati3192 – 322938Plectin 8Add
BLAST
Repeati3230 – 326738Plectin 9Add
BLAST
Repeati3268 – 330538Plectin 10Add
BLAST
Repeati3306 – 334338Plectin 11Add
BLAST
Repeati3485 – 352238Plectin 12Add
BLAST
Repeati3523 – 356038Plectin 13Add
BLAST
Repeati3561 – 359838Plectin 14Add
BLAST
Repeati3599 – 363638Plectin 15Add
BLAST
Repeati3640 – 367435Plectin 16Add
BLAST
Repeati3820 – 385738Plectin 17Add
BLAST
Repeati3858 – 389538Plectin 18Add
BLAST
Repeati3896 – 393338Plectin 19Add
BLAST
Repeati3934 – 397138Plectin 20Add
BLAST
Repeati3975 – 400834Plectin 21Add
BLAST
Repeati4063 – 410038Plectin 22Add
BLAST
Repeati4101 – 413838Plectin 23Add
BLAST
Repeati4139 – 417638Plectin 24Add
BLAST
Repeati4177 – 421438Plectin 25Add
BLAST
Repeati4218 – 425235Plectin 26Add
BLAST
Repeati4265 – 430541Plectin 27Add
BLAST
Repeati4319 – 435638Plectin 28Add
BLAST
Repeati4408 – 444538Plectin 29Add
BLAST
Repeati4446 – 448338Plectin 30Add
BLAST
Repeati4484 – 452138Plectin 31Add
BLAST
Repeati4522 – 455938Plectin 32Add
BLAST
Repeati4560 – 459738Plectin 33Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 14701470Globular 1Add
BLAST
Regioni1471 – 27551285Central fibrous rod domainAdd
BLAST
Regioni2756 – 46841929Globular 2Add
BLAST
Regioni4250 – 430051Binding to intermediate filamentsBy similarityAdd
BLAST
Regioni4625 – 4640164 X 4 AA tandem repeats of G-S-R-XAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1469 – 27561288Sequence AnalysisAdd
BLAST

Domaini

The N-terminus interacts with actin, the C-terminus with vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N- and the C-terminus can bind integrin beta-4.

Sequence similaritiesi

Belongs to the plakin or cytolinker family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 33 plectin repeats.Curated
Contains 4 spectrin repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00760000119163.
HOVERGENiHBG053616.
InParanoidiQ15149.
KOiK10388.
OMAiYLNKDTH.
PhylomeDBiQ15149.
TreeFamiTF335163.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
3.90.1290.10. 7 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001101. Plectin_repeat.
IPR005326. S10_plectin_N.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00681. Plectin. 18 hits.
PF03501. S10_plectin. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00250. PLEC. 32 hits.
SM00150. SPEC. 7 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 8 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15149-1) [UniParc]FASTAAdd to Basket

Also known as: Plectin-6

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVAGMLMPRD QLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR
60 70 80 90 100
AMASLRARGL VRETFAWCHF YWYLTNEGIA HLRQYLHLPP EIVPASLQRV
110 120 130 140 150
RRPVAMVMPA RRTPHVQAVQ GPLGSPPKRG PLPTEEQRVY RRKELEEVSP
160 170 180 190 200
ETPVVPATTQ RTLARPGPEP APATDERDRV QKKTFTKWVN KHLIKAQRHI
210 220 230 240 250
SDLYEDLRDG HNLISLLEVL SGDSLPREKG RMRFHKLQNV QIALDYLRHR
260 270 280 290 300
QVKLVNIRND DIADGNPKLT LGLIWTIILH FQISDIQVSG QSEDMTAKEK
310 320 330 340 350
LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ
360 370 380 390 400
TNLENLDQAF SVAERDLGVT RLLDPEDVDV PQPDEKSIIT YVSSLYDAMP
410 420 430 440 450
RVPDVQDGVR ANELQLRWQE YRELVLLLLQ WMRHHTAAFE ERRFPSSFEE
460 470 480 490 500
IEILWSQFLK FKEMELPAKE ADKNRSKGIY QSLEGAVQAG QLKVPPGYHP
510 520 530 540 550
LDVEKEWGKL HVAILEREKQ LRSEFERLEC LQRIVTKLQM EAGLCEEQLN
560 570 580 590 600
QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF NDVQTLKDGR
610 620 630 640 650
HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR
660 670 680 690 700
RPELEDSTLR YLQDLLAWVE ENQHRVDGAE WGVDLPSVEA QLGSHRGLHQ
710 720 730 740 750
SIEEFRAKIE RARSDEGQLS PATRGAYRDC LGRLDLQYAK LLNSSKARLR
760 770 780 790 800
SLESLHSFVA AATKELMWLN EKEEEEVGFD WSDRNTNMTA KKESYSALMR
810 820 830 840 850
ELELKEKKIK ELQNAGDRLL REDHPARPTV ESFQAALQTQ WSWMLQLCCC
860 870 880 890 900
IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR SATVTRLEDL
910 920 930 940 950
LQDAQDEKEQ LNEYKGHLSG LAKRAKAVVQ LKPRHPAHPM RGRLPLLAVC
960 970 980 990 1000
DYKQVEVTVH KGDECQLVGP AQPSHWKVLS SSGSEAAVPS VCFLVPPPNQ
1010 1020 1030 1040 1050
EAQEAVTRLE AQHQALVTLW HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT
1060 1070 1080 1090 1100
FRTLKPEEQR QALHSLELHY QAFLRDSQDA GGFGPEDRLM AEREYGSCSH
1110 1120 1130 1140 1150
HYQQLLQSLE QGAQEESRCQ RCISELKDIR LQLEACETRT VHRLRLPLDK
1160 1170 1180 1190 1200
EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL PEPSPAAPTL
1210 1220 1230 1240 1250
RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK
1260 1270 1280 1290 1300
EAQAVPATLP ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL
1310 1320 1330 1340 1350
QQRHGERDVE VERWRERVAQ LLERWQAVLA QTDVRQRELE QLGRQLRYYR
1360 1370 1380 1390 1400
ESADPLGAWL QDARRRQEQI QAMPLADSQA VREQLRQEQA LLEEIERHGE
1410 1420 1430 1440 1450
KVEECQRFAK QYINAIKDYE LQLVTYKAQL EPVASPAKKP KVQSGSESVI
1460 1470 1480 1490 1500
QEYVDLRTHY SELTTLTSQY IKFISETLRR MEEEERLAEQ QRAEERERLA
1510 1520 1530 1540 1550
EVEAALEKQR QLAEAHAQAK AQAEREAKEL QQRMQEEVVR REEAAVDAQQ
1560 1570 1580 1590 1600
QKRSIQEELQ QLRQSSEAEI QAKARQAEAA ERSRLRIEEE IRVVRLQLEA
1610 1620 1630 1640 1650
TERQRGGAEG ELQALRARAE EAEAQKRQAQ EEAERLRRQV QDESQRKRQA
1660 1670 1680 1690 1700
EVELASRVKA EAEAAREKQR ALQALEELRL QAEEAERRLR QAEVERARQV
1710 1720 1730 1740 1750
QVALETAQRS AEAELQSKRA SFAEKTAQLE RSLQEEHVAV AQLREEAERR
1760 1770 1780 1790 1800
AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ QKSLAQAEAE
1810 1820 1830 1840 1850
KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ
1860 1870 1880 1890 1900
ELIRLRAETE QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE
1910 1920 1930 1940 1950
MEVLLASKAR AEEESRSTSE KSKQRLEAEA GRFRELAEEA ARLRALAEEA
1960 1970 1980 1990 2000
KRQRQLAEED AARQRAEAER VLAEKLAAIG EATRLKTEAE IALKEKEAEN
2010 2020 2030 2040 2050
ERLRRLAEDE AFQRRRLEEQ AAQHKADIEE RLAQLRKASD SELERQKGLV
2060 2070 2080 2090 2100
EDTLRQRRQV EEEILALKAS FEKAAAGKAE LELELGRIRS NAEDTLRSKE
2110 2120 2130 2140 2150
QAELEAARQR QLAAEEERRR REAEERVQKS LAAEEEAARQ RKAALEEVER
2160 2170 2180 2190 2200
LKAKVEEARR LRERAEQESA RQLQLAQEAA QKRLQAEEKA HAFAVQQKEQ
2210 2220 2230 2240 2250
ELQQTLQQEQ SVLDQLRGEA EAARRAAEEA EEARVQAERE AAQSRRQVEE
2260 2270 2280 2290 2300
AERLKQSAEE QAQARAQAQA AAEKLRKEAE QEAARRAQAE QAALRQKQAA
2310 2320 2330 2340 2350
DAEMEKHKKF AEQTLRQKAQ VEQELTTLRL QLEETDHQKN LLDEELQRLK
2360 2370 2380 2390 2400
AEATEAARQR SQVEEELFSV RVQMEELSKL KARIEAENRA LILRDKDNTQ
2410 2420 2430 2440 2450
RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK
2460 2470 2480 2490 2500
EKMQAVQEAT RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG
2510 2520 2530 2540 2550
FQRTLEAERQ RQLEMSAEAE RLKLRVAEMS RAQARAEEDA QRFRKQAEEI
2560 2570 2580 2590 2600
GEKLHRTELA TQEKVTLVQT LEIQRQQSDH DAERLREAIA ELEREKEKLQ
2610 2620 2630 2640 2650
QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ SFLSEKDSLL QRERFIEQEK
2660 2670 2680 2690 2700
AKLEQLFQDE VAKAQQLREE QQRQQQQMEQ ERQRLVASME EARRRQHEAE
2710 2720 2730 2740 2750
EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE
2760 2770 2780 2790 2800
EVTASQVAAT KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI
2810 2820 2830 2840 2850
LSAEELQRLA QGHTTVDELA RREDVRHYLQ GRSSIAGLLL KATNEKLSVY
2860 2870 2880 2890 2900
AALQRQLLSP GTALILLEAQ AASGFLLDPV RNRRLTVNEA VKEGVVGPEL
2910 2920 2930 2940 2950
HHKLLSAERA VTGYKDPYTG QQISLFQAMQ KGLIVREHGI RLLEAQIATG
2960 2970 2980 2990 3000
GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT
3010 3020 3030 3040 3050
YLQLLERCVE DPETGLCLLP LTDKAAKGGE LVYTDSEARD VFEKATVSAP
3060 3070 3080 3090 3100
FGKFQGKTVT IWEIINSEYF TAEQRRDLLR QFRTGRITVE KIIKIIITVV
3110 3120 3130 3140 3150
EEQEQKGRLC FEGLRSLVPA AELLESRVID RELYQQLQRG ERSVRDVAEV
3160 3170 3180 3190 3200
DTVRRALRGA NVIAGVWLEE AGQKLSIYNA LKKDLLPSDM AVALLEAQAG
3210 3220 3230 3240 3250
TGHIIDPATS ARLTVDEAVR AGLVGPEFHE KLLSAEKAVT GYRDPYTGQS
3260 3270 3280 3290 3300
VSLFQALKKG LIPREQGLRL LDAQLSTGGI VDPSKSHRVP LDVACARGCL
3310 3320 3330 3340 3350
DEETSRALSA PRADAKAYSD PSTGEPATYG ELQQRCRPDQ LTGLSLLPLS
3360 3370 3380 3390 3400
EKAARARQEE LYSELQARET FEKTPVEVPV GGFKGRTVTV WELISSEYFT
3410 3420 3430 3440 3450
AEQRQELLRQ FRTGKVTVEK VIKILITIVE EVETLRQERL SFSGLRAPVP
3460 3470 3480 3490 3500
ASELLASGVL SRAQFEQLKD GKTTVKDLSE LGSVRTLLQG SGCLAGIYLE
3510 3520 3530 3540 3550
DTKEKVSIYE AMRRGLLRAT TAALLLEAQA ATGFLVDPVR NQRLYVHEAV
3560 3570 3580 3590 3600
KAGVVGPELH EQLLSAEKAV TGYRDPYSGS TISLFQAMQK GLVLRQHGIR
3610 3620 3630 3640 3650
LLEAQIATGG IIDPVHSHRV PVDVAYQRGY FSEEMNRVLA DPSDDTKGFF
3660 3670 3680 3690 3700
DPNTHENLTY RQLLERCVED PETGLRLLPL KGAEKAEVVE TTQVYTEEET
3710 3720 3730 3740 3750
RRAFEETQID IPGGGSHGGS TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV
3760 3770 3780 3790 3800
TKERMIIIII EIIEKTEIIR QQGLASYDYV RRRLTAEDLF EARIISLETY
3810 3820 3830 3840 3850
NLLREGTRSL REALEAESAW CYLYGTGSVA GVYLPGSRQT LSIYQALKKG
3860 3870 3880 3890 3900
LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV GPELHDRLLS
3910 3920 3930 3940 3950
AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR
3960 3970 3980 3990 4000
LGFHLPLEVA YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR
4010 4020 4030 4040 4050
CRRDDGTGQL LLPLSDARKL TFRGLRKQIT MEELVRSQVM DEATALQLRE
4060 4070 4080 4090 4100
GLTSIEEVTK NLQKFLEGTS CIAGVFVDAT KERLSVYQAM KKGIIRPGTA
4110 4120 4130 4140 4150
FELLEAQAAT GYVIDPIKGL KLTVEEAVRM GIVGPEFKDK LLSAERAVTG
4160 4170 4180 4190 4200
YKDPYSGKLI SLFQAMKKGL ILKDHGIRLL EAQIATGGII DPEESHRLPV
4210 4220 4230 4240 4250
EVAYKRGLFD EEMNEILTDP SDDTKGFFDP NTEENLTYLQ LMERCITDPQ
4260 4270 4280 4290 4300
TGLCLLPLKE KKRERKTSSK SSVRKRRVVI VDPETGKEMS VYEAYRKGLI
4310 4320 4330 4340 4350
DHQTYLELSE QECEWEEITI SSSDGVVKSM IIDRRSGRQY DIDDAIAKNL
4360 4370 4380 4390 4400
IDRSALDQYR AGTLSITEFA DMLSGNAGGF RSRSSSVGSS SSYPISPAVS
4410 4420 4430 4440 4450
RTQLASWSDP TEETGPVAGI LDTETLEKVS ITEAMHRNLV DNITGQRLLE
4460 4470 4480 4490 4500
AQACTGGIID PSTGERFPVT DAVNKGLVDK IMVDRINLAQ KAFCGFEDPR
4510 4520 4530 4540 4550
TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ
4560 4570 4580 4590 4600
RGTVDARTAQ KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL
4610 4620 4630 4640 4650
LEAAAQSTKG YYSPYSVSGS GSTAGSRTGS RTGSRAGSRR GSFDATGSGF
4660 4670 4680
SMTFSSSSYS SSGYGRRYAS GSSASLGGPE SAVA
Length:4,684
Mass (Da):531,791
Last modified:October 14, 2008 - v3
Checksum:i04772E4F70A304C8
GO
Isoform 2 (identifier: Q15149-2) [UniParc]FASTAAdd to Basket

Also known as: Plectin-1, 1c

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA

Note: Contains a phosphoserine at position 42.

Show »
Length:4,574
Mass (Da):518,473
Checksum:i7EAEA5A83DEF52EA
GO
Isoform 3 (identifier: Q15149-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA
     409-412: Missing.

Note: Contains a phosphoserine at position 42.

Show »
Length:4,570
Mass (Da):518,032
Checksum:iA0AF260B8C095C8D
GO
Isoform 4 (identifier: Q15149-4) [UniParc]FASTAAdd to Basket

Also known as: Plectin-11, 1a

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSQHQLRVPQ...AVLRASEGKK

Note: Contains a phosphotyrosine at position 26 (By similarity). Contains a phosphoserine at position 21. Contains a phosphoserine at position 20.By similarity

Show »
Length:4,547
Mass (Da):516,198
Checksum:i0A1A2AB2E557110A
GO
Isoform 5 (identifier: Q15149-5) [UniParc]FASTAAdd to Basket

Also known as: Plectin-8, 1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.
     138-174: RVYRRKELEEVSPETPVVPATTQRTLARPGPEPAPAT → MEPSGSLFPSLVVVGHVVTLAAVWHWRRGRRWAQDEQ

Show »
Length:4,547
Mass (Da):516,276
Checksum:i0EC98F109B723779
GO
Isoform 6 (identifier: Q15149-6) [UniParc]FASTAAdd to Basket

Also known as: Plectin-10, 1g

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     134-174: TEEQRVYRRK...RPGPEPAPAT → MSGAGGAFAS...GYLYQQLCCV

Show »
Length:4,551
Mass (Da):516,479
Checksum:iC2E0FDA51BC17BF2
GO
Isoform 7 (identifier: Q15149-7) [UniParc]FASTAAdd to Basket

Also known as: Plectin-7, 1d

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: Missing.
     170-174: PAPAT → MKIVP

Show »
Length:4,515
Mass (Da):512,604
Checksum:iC8701AD6D1C1B26E
GO
Isoform 8 (identifier: Q15149-8) [UniParc]FASTAAdd to Basket

Also known as: Plectin-3, 1e

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
     160-174: QRTLARPGPEPAPAT → MDPSRAIQNEISSLK

Show »
Length:4,525
Mass (Da):513,706
Checksum:i37A4DFAB46C3B4DD
GO
Isoform 9 (identifier: Q15149-9) [UniParc]FASTAAdd to Basket

Also known as: Plectin-2, 1f

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.
     152-174: TPVVPATTQRTLARPGPEPAPAT → MAGPLPDEQDFIQAYEEVREKYK

Show »
Length:4,533
Mass (Da):514,775
Checksum:i5D6382389A66B955
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711Y → F in CAA91196. (PubMed:8633055)Curated
Sequence conflicti94 – 941P → A in CAA91196. (PubMed:8633055)Curated
Sequence conflicti139 – 1391V → L in CAA91196. (PubMed:8633055)Curated
Sequence conflicti185 – 1851F → S in CAA91196. (PubMed:8633055)Curated
Sequence conflicti259 – 2591N → D in AAB05427. (PubMed:8698233)Curated
Sequence conflicti259 – 2591N → D in AAB05428. (PubMed:8698233)Curated
Sequence conflicti550 – 5501N → H in CAA91196. (PubMed:8633055)Curated
Sequence conflicti560 – 5601V → I in CAA91196. (PubMed:8633055)Curated
Sequence conflicti706 – 7061R → Q in CAA91196. (PubMed:8633055)Curated
Sequence conflicti886 – 8861Y → N in CAA91196. (PubMed:8633055)Curated
Sequence conflicti1002 – 10021A → V in CAA91196. (PubMed:8633055)Curated
Sequence conflicti1309 – 13091V → L in AAB05427. (PubMed:8698233)Curated
Sequence conflicti1309 – 13091V → L in AAB05428. (PubMed:8698233)Curated
Sequence conflicti1334 – 13341V → L in AAB05427. (PubMed:8698233)Curated
Sequence conflicti1334 – 13341V → L in AAB05428. (PubMed:8698233)Curated
Sequence conflicti1534 – 15341M → I in CAA91196. (PubMed:8633055)Curated
Sequence conflicti1662 – 16621A → T in AAB05427. (PubMed:8698233)Curated
Sequence conflicti1662 – 16621A → T in AAB05428. (PubMed:8698233)Curated
Sequence conflicti1688 – 16903RLR → WLC in CAA91196. (PubMed:8633055)Curated
Sequence conflicti1767 – 17671E → Q in CAA91196. (PubMed:8633055)Curated
Sequence conflicti1789 – 17891A → L in CAA91196. (PubMed:8633055)Curated
Sequence conflicti1910 – 19101R → K in CAA91196. (PubMed:8633055)Curated
Sequence conflicti2154 – 21541K → N in AAB05427. (PubMed:8698233)Curated
Sequence conflicti2154 – 21541K → N in AAB05428. (PubMed:8698233)Curated
Sequence conflicti2154 – 21541K → N in CAA65765. (PubMed:8698233)Curated
Sequence conflicti2154 – 21541K → N in AAR95680. (PubMed:14672974)Curated
Sequence conflicti2154 – 21541K → N in AAR95682. (PubMed:14672974)Curated
Sequence conflicti2154 – 21541K → N in AAR95683. (PubMed:14672974)Curated
Sequence conflicti2160 – 21601R → S in CAA91196. (PubMed:8633055)Curated
Sequence conflicti2215 – 22151Q → R in CAA91196. (PubMed:8633055)Curated
Sequence conflicti2244 – 22441S → A in CAA91196. (PubMed:8633055)Curated
Sequence conflicti2244 – 22441S → A in AAB05427. (PubMed:8698233)Curated
Sequence conflicti2244 – 22441S → A in AAB05428. (PubMed:8698233)Curated
Sequence conflicti2244 – 22441S → A in CAA65765. (PubMed:8698233)Curated
Sequence conflicti3027 – 30271K → E in AAB05427. (PubMed:8698233)Curated
Sequence conflicti3027 – 30271K → E in AAB05428. (PubMed:8698233)Curated
Sequence conflicti3310 – 33101A → E in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3361 – 33611L → F in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3408 – 34081L → F in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3447 – 34471A → S in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3531 – 35311A → G in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3580 – 35801S → R in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3589 – 35891Q → K in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3596 – 35961Q → E in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3616 – 36161H → N in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3686 – 36861A → V in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3786 – 37861A → G in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3808 – 38081R → K in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3816 – 38161A → G in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3821 – 38211C → F in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3915 – 39151Q → K in CAA91196. (PubMed:8633055)Curated
Sequence conflicti3999 – 39991R → K in CAA91196. (PubMed:8633055)Curated
Sequence conflicti4007 – 40071T → S in CAA91196. (PubMed:8633055)Curated
Sequence conflicti4467 – 44671F → L in CAA91196. (PubMed:8633055)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti429 – 4291L → LL in MD-EBS. 1 Publication
VAR_011336
Natural varianti641 – 6411A → V.
Corresponds to variant rs11136336 [ dbSNP | Ensembl ].
VAR_053585
Natural varianti1003 – 10053Missing in MD-EBS. 1 Publication
VAR_011337
Natural varianti1321 – 13211L → V.1 Publication
Corresponds to variant rs3135109 [ dbSNP | Ensembl ].
VAR_060088
Natural varianti1386 – 13861R → Q.
Corresponds to variant rs11136334 [ dbSNP | Ensembl ].
VAR_060089
Natural varianti1459 – 14591H → R.
Corresponds to variant rs55895668 [ dbSNP | Ensembl ].
VAR_062133
Natural varianti2110 – 21101R → W in O-EBS. 1 Publication
VAR_015817
Natural varianti2150 – 21501R → W.
Corresponds to variant rs34893635 [ dbSNP | Ensembl ].
VAR_053586
Natural varianti2194 – 21941A → V.
Corresponds to variant rs7002002 [ dbSNP | Ensembl ].
VAR_053587
Natural varianti2791 – 27911S → P.
Corresponds to variant rs7833924 [ dbSNP | Ensembl ].
VAR_053588
Natural varianti2821 – 28211R → W.
Corresponds to variant rs35723243 [ dbSNP | Ensembl ].
VAR_053589
Natural varianti2969 – 29691R → H.
Corresponds to variant rs6558407 [ dbSNP | Ensembl ].
VAR_053590
Natural varianti3162 – 31621V → I.
Corresponds to variant rs35027700 [ dbSNP | Ensembl ].
VAR_053591
Natural varianti3171 – 31711A → V.
Corresponds to variant rs35858667 [ dbSNP | Ensembl ].
VAR_053592
Natural varianti3486 – 34861T → M.
Corresponds to variant rs34725742 [ dbSNP | Ensembl ].
VAR_053593
Natural varianti3490 – 34901G → A.
Corresponds to variant rs35261863 [ dbSNP | Ensembl ].
VAR_053594

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 174174MVAGM…PAPAT → MSGEDAEVRAVSEDVSNGSS GSPSPGDTLPWNLGKTQRSR RSGGGAGSNGSVLDPAERAV IRIA in isoform 2 and isoform 3. 2 PublicationsVSP_005030Add
BLAST
Alternative sequencei1 – 174174MVAGM…PAPAT → MSQHQLRVPQPEGLGRKRTS SEDNLYLAVLRASEGKK in isoform 4. 1 PublicationVSP_023510Add
BLAST
Alternative sequencei1 – 169169Missing in isoform 7. 1 PublicationVSP_037100Add
BLAST
Alternative sequencei1 – 159159Missing in isoform 8. 1 PublicationVSP_037101Add
BLAST
Alternative sequencei1 – 151151Missing in isoform 9. 1 PublicationVSP_037102Add
BLAST
Alternative sequencei1 – 137137Missing in isoform 5. 1 PublicationVSP_037103Add
BLAST
Alternative sequencei1 – 133133Missing in isoform 6. 1 PublicationVSP_037104Add
BLAST
Alternative sequencei134 – 17441TEEQR…PAPAT → MSGAGGAFASPREVLLERPC WLDGGCEPARRGYLYQQLCC V in isoform 6. 1 PublicationVSP_037105Add
BLAST
Alternative sequencei138 – 17437RVYRR…PAPAT → MEPSGSLFPSLVVVGHVVTL AAVWHWRRGRRWAQDEQ in isoform 5. 1 PublicationVSP_037106Add
BLAST
Alternative sequencei152 – 17423TPVVP…PAPAT → MAGPLPDEQDFIQAYEEVRE KYK in isoform 9. 1 PublicationVSP_037107Add
BLAST
Alternative sequencei160 – 17415QRTLA…PAPAT → MDPSRAIQNEISSLK in isoform 8. 1 PublicationVSP_037108Add
BLAST
Alternative sequencei170 – 1745PAPAT → MKIVP in isoform 7. 1 PublicationVSP_037109
Alternative sequencei409 – 4124Missing in isoform 3. 1 PublicationVSP_005031

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z54367 Genomic DNA. Translation: CAA91196.1.
U53204 mRNA. Translation: AAB05427.1.
U63610, U63609 Genomic DNA. Translation: AAB05428.1.
X97053 mRNA. Translation: CAA65765.1.
AY480044 mRNA. Translation: AAR95677.1.
AY480045 mRNA. Translation: AAR95678.1.
AY480046 mRNA. Translation: AAR95679.1.
AY480047 mRNA. Translation: AAR95680.1.
AY480048 mRNA. Translation: AAR95681.1.
AY480049 mRNA. Translation: AAR95682.1.
AY480050 mRNA. Translation: AAR95683.1.
AY480051 mRNA. Translation: AAR95684.1.
AC109322 Genomic DNA. No translation available.
CCDSiCCDS43769.1. [Q15149-2]
CCDS43770.1. [Q15149-9]
CCDS43771.1. [Q15149-8]
CCDS43772.1. [Q15149-1]
CCDS43773.1. [Q15149-5]
CCDS43774.1. [Q15149-6]
CCDS43775.1. [Q15149-4]
CCDS47936.1. [Q15149-7]
PIRiC59404. A59404.
G02520.
RefSeqiNP_000436.2. NM_000445.4. [Q15149-2]
NP_958780.1. NM_201378.3. [Q15149-9]
NP_958781.1. NM_201379.2. [Q15149-8]
NP_958782.1. NM_201380.3. [Q15149-1]
NP_958783.1. NM_201381.2. [Q15149-7]
NP_958784.1. NM_201382.3. [Q15149-5]
NP_958785.1. NM_201383.2. [Q15149-6]
NP_958786.1. NM_201384.2. [Q15149-4]
UniGeneiHs.434248.

Genome annotation databases

EnsembliENST00000322810; ENSP00000323856; ENSG00000178209. [Q15149-1]
ENST00000345136; ENSP00000344848; ENSG00000178209. [Q15149-4]
ENST00000354589; ENSP00000346602; ENSG00000178209. [Q15149-5]
ENST00000354958; ENSP00000347044; ENSG00000178209. [Q15149-8]
ENST00000356346; ENSP00000348702; ENSG00000178209. [Q15149-9]
ENST00000357649; ENSP00000350277; ENSG00000178209. [Q15149-6]
ENST00000398774; ENSP00000381756; ENSG00000178209. [Q15149-7]
ENST00000436759; ENSP00000388180; ENSG00000178209. [Q15149-2]
ENST00000527096; ENSP00000434583; ENSG00000178209. [Q15149-3]
GeneIDi5339.
KEGGihsa:5339.
UCSCiuc003zab.1. human. [Q15149-4]
uc003zac.1. human. [Q15149-6]
uc003zad.2. human. [Q15149-5]
uc003zae.1. human. [Q15149-7]
uc003zaf.1. human. [Q15149-1]
uc003zag.1. human. [Q15149-8]
uc003zah.2. human. [Q15149-9]
uc003zaj.2. human. [Q15149-2]

Polymorphism databases

DMDMi209572726.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Plectin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z54367 Genomic DNA. Translation: CAA91196.1 .
U53204 mRNA. Translation: AAB05427.1 .
U63610 , U63609 Genomic DNA. Translation: AAB05428.1 .
X97053 mRNA. Translation: CAA65765.1 .
AY480044 mRNA. Translation: AAR95677.1 .
AY480045 mRNA. Translation: AAR95678.1 .
AY480046 mRNA. Translation: AAR95679.1 .
AY480047 mRNA. Translation: AAR95680.1 .
AY480048 mRNA. Translation: AAR95681.1 .
AY480049 mRNA. Translation: AAR95682.1 .
AY480050 mRNA. Translation: AAR95683.1 .
AY480051 mRNA. Translation: AAR95684.1 .
AC109322 Genomic DNA. No translation available.
CCDSi CCDS43769.1. [Q15149-2 ]
CCDS43770.1. [Q15149-9 ]
CCDS43771.1. [Q15149-8 ]
CCDS43772.1. [Q15149-1 ]
CCDS43773.1. [Q15149-5 ]
CCDS43774.1. [Q15149-6 ]
CCDS43775.1. [Q15149-4 ]
CCDS47936.1. [Q15149-7 ]
PIRi C59404. A59404.
G02520.
RefSeqi NP_000436.2. NM_000445.4. [Q15149-2 ]
NP_958780.1. NM_201378.3. [Q15149-9 ]
NP_958781.1. NM_201379.2. [Q15149-8 ]
NP_958782.1. NM_201380.3. [Q15149-1 ]
NP_958783.1. NM_201381.2. [Q15149-7 ]
NP_958784.1. NM_201382.3. [Q15149-5 ]
NP_958785.1. NM_201383.2. [Q15149-6 ]
NP_958786.1. NM_201384.2. [Q15149-4 ]
UniGenei Hs.434248.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MB8 X-ray 2.15 A 175-403 [» ]
2ODU X-ray 2.30 A 410-640 [» ]
2ODV X-ray 2.05 A 410-640 [» ]
3F7P X-ray 2.75 A/B 175-403 [» ]
3PDY X-ray 2.22 A/B 653-858 [» ]
3PE0 X-ray 2.95 A/B 750-1028 [» ]
4GDO X-ray 1.70 A/B/C/D/E/F 1492-1530 [» ]
4Q58 X-ray 4.00 A/B 175-400 [» ]
4Q59 X-ray 2.30 A/B 175-400 [» ]
ProteinModelPortali Q15149.
SMRi Q15149. Positions 5-101, 175-400, 413-630, 653-1025, 2782-3023, 3441-3681, 4021-4260, 4412-4605.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111355. 62 interactions.
IntActi Q15149. 25 interactions.
MINTi MINT-257064.

Chemistry

BindingDBi Q15149.
ChEMBLi CHEMBL1293240.

PTM databases

PhosphoSitei Q15149.

Polymorphism databases

DMDMi 209572726.

Proteomic databases

MaxQBi Q15149.
PaxDbi Q15149.
PRIDEi Q15149.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322810 ; ENSP00000323856 ; ENSG00000178209 . [Q15149-1 ]
ENST00000345136 ; ENSP00000344848 ; ENSG00000178209 . [Q15149-4 ]
ENST00000354589 ; ENSP00000346602 ; ENSG00000178209 . [Q15149-5 ]
ENST00000354958 ; ENSP00000347044 ; ENSG00000178209 . [Q15149-8 ]
ENST00000356346 ; ENSP00000348702 ; ENSG00000178209 . [Q15149-9 ]
ENST00000357649 ; ENSP00000350277 ; ENSG00000178209 . [Q15149-6 ]
ENST00000398774 ; ENSP00000381756 ; ENSG00000178209 . [Q15149-7 ]
ENST00000436759 ; ENSP00000388180 ; ENSG00000178209 . [Q15149-2 ]
ENST00000527096 ; ENSP00000434583 ; ENSG00000178209 . [Q15149-3 ]
GeneIDi 5339.
KEGGi hsa:5339.
UCSCi uc003zab.1. human. [Q15149-4 ]
uc003zac.1. human. [Q15149-6 ]
uc003zad.2. human. [Q15149-5 ]
uc003zae.1. human. [Q15149-7 ]
uc003zaf.1. human. [Q15149-1 ]
uc003zag.1. human. [Q15149-8 ]
uc003zah.2. human. [Q15149-9 ]
uc003zaj.2. human. [Q15149-2 ]

Organism-specific databases

CTDi 5339.
GeneCardsi GC08M144989.
GeneReviewsi PLEC.
H-InvDB HIX0168901.
HGNCi HGNC:9069. PLEC.
HPAi CAB003847.
HPA025967.
HPA029906.
MIMi 131950. phenotype.
226670. phenotype.
601282. gene.
612138. phenotype.
613723. phenotype.
neXtProti NX_Q15149.
Orphaneti 254361. Autosomal recessive limb-girdle muscular dystrophy type 2Q.
257. Epidermolysis bullosa simplex with muscular dystrophy.
158684. Epidermolysis bullosa simplex with pyloric atresia.
79401. Epidermolysis bullosa simplex, Ogna type.
PharmGKBi PA33399.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000119163.
HOVERGENi HBG053616.
InParanoidi Q15149.
KOi K10388.
OMAi YLNKDTH.
PhylomeDBi Q15149.
TreeFami TF335163.

Enzyme and pathway databases

Reactomei REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_20537. Type I hemidesmosome assembly.

Miscellaneous databases

ChiTaRSi PLEC. human.
EvolutionaryTracei Q15149.
GeneWikii Plectin.
GenomeRNAii 5339.
NextBioi 20680.
PROi Q15149.
SOURCEi Search...

Gene expression databases

Bgeei Q15149.
CleanExi HS_PLEC1.
ExpressionAtlasi Q15149. baseline and differential.
Genevestigatori Q15149.

Family and domain databases

Gene3Di 1.10.418.10. 2 hits.
3.90.1290.10. 7 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001101. Plectin_repeat.
IPR005326. S10_plectin_N.
IPR018159. Spectrin/alpha-actinin.
[Graphical view ]
Pfami PF00307. CH. 2 hits.
PF00681. Plectin. 18 hits.
PF03501. S10_plectin. 1 hit.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00250. PLEC. 32 hits.
SM00150. SPEC. 7 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 8 hits.
PROSITEi PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24)."
    Liu C.-G., Maercker C., Castanon M.J., Hauptmann R., Wiche G.
    Proc. Natl. Acad. Sci. U.S.A. 93:4278-4283(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), DISEASE, VARIANT VAL-1321.
  3. "Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation."
    Zhang T., Haws P., Wu Q.
    Genome Res. 14:79-89(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7; 8 AND 9).
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Tissue: Ovarian carcinoma.
  6. "Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly."
    Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.
    J. Cell Sci. 116:387-399(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COL17A1, SUBCELLULAR LOCATION.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-1435; SER-1721; THR-4030 AND THR-4411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-4382; SER-4385; SER-4386; SER-4389; SER-4390; SER-4391; SER-4392; SER-4396; SER-4613; SER-4622; SER-4626 AND SER-4642, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
    Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
    J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOR1A.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; THR-4030 AND SER-4626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4386; SER-4389; SER-4396; SER-4613; SER-4618 AND SER-4626, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3091 AND LYS-3420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f, causes autosomal-recessive limb-girdle muscular dystrophy."
    Gundesli H., Talim B., Korkusuz P., Balci-Hayta B., Cirak S., Akarsu N.A., Topaloglu H., Dincer P.
    Am. J. Hum. Genet. 87:834-841(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF ISOFORM 9, INVOLVEMENT IN LGMD2Q.
  19. "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
    Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
    Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DST.
  20. "Plectin deficiency leads to both muscular dystrophy and pyloric atresia in epidermolysis bullosa simplex."
    Natsuga K., Nishie W., Shinkuma S., Arita K., Nakamura H., Ohyama M., Osaka H., Kambara T., Hirako Y., Shimizu H.
    Hum. Mutat. 31:E1687-E1698(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MD-EBS AND EBS-PA.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113; SER-125; SER-149; SER-720; SER-1435; SER-1732; THR-4030; SER-4382; SER-4396; SER-4400; SER-4613; SER-4622 AND SER-4642, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-21 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C."
    Maiweilidan Y., Klauza I., Kordeli E.
    Exp. Cell Res. 317:724-736(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANK3.
  24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435 AND THR-4030, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain."
    Sonnenberg A., Rojas A.M., de Pereda J.M.
    J. Mol. Biol. 368:1379-1391(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 409-640.
  26. "Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4."
    Garcia-Alvarez B., Bobkov A., Sonnenberg A., de Pereda J.M.
    Structure 11:615-625(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 159-403.
  27. "Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy."
    Pulkkinen L., Smith F.J.D., Shimizu H., Murata S., Yaoita H., Hachisuka H., Nishikawa T., McLean W.H.I., Uitto J.
    Hum. Mol. Genet. 5:1539-1546(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MD-EBS 1003-GLN--ALA-1005 DEL.
  28. "A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency."
    Bauer J.W., Rouan F., Kofler B., Rezniczek G.A., Kornacker I., Muss W., Hametner R., Klausegger A., Huber A., Pohla-Gubo G., Wiche G., Uitto J., Hintner H.
    Am. J. Pathol. 158:617-625(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MD-EBS LEU-429 INS.
  29. "A site-specific plectin mutation causes dominant epidermolysis bullosa simplex Ogna: two identical de novo mutations."
    Koss-Harnes D., Hoeyheim B., Anton-Lamprecht I., Gjesti A., Joergensen R.S., Jahnsen F.L., Olaisen B., Wiche G., Gedde-Dahl T. Jr.
    J. Invest. Dermatol. 118:87-93(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT O-EBS TRP-2110.
  30. "Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin."
    Charlesworth A., Gagnoux-Palacios L., Bonduelle M., Ortonne J.-P., De Raeve L., Meneguzzi G.
    J. Invest. Dermatol. 121:1344-1348(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN EBS-PA.

Entry informationi

Entry nameiPLEC_HUMAN
AccessioniPrimary (citable) accession number: Q15149
Secondary accession number(s): Q15148
, Q16640, Q6S376, Q6S377, Q6S378, Q6S379, Q6S380, Q6S381, Q6S382, Q6S383
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3